BCH210H1 Lecture Notes - Lecture 4: Collagen, Triple Helix, Microfibril

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Reinhart Reithmeier

Document Summary

Between the carbon (carbonyl) and nitrogen (amine: c n. Resonance: carbonyl group has a double bond resonance, c n has double bond character, cannot rotate- rigid, has cis-trans conformations, carbon backbones are 180 from each other, planar. Trans conformation: forms characteristic angles (phi-psi angles, minimize steric hindrance. Between c n bond (peptide bond) (cid:523) [chi angle] By finding the angles of the amino acids they always fall into and angles. Alanine in 3d: can exist in and conformations not restricted. Glycine in 3d: little in , little in . Mainly found in l conformation: left-handed -helical turns. When protein has lots of l angles most often glycine: small & compact. Carbonyl group pokes into/out of the structure: makes a conformational difference, both exist in nature. Oth and conformations: ut distorted. Distorted -angles polyproline helices: polyproline helices are not -helices, no hydrogen bonds b/w structure very different from -helix) Wool: high in cysteine (disulphide bonds) & glutamate & serine.